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P00636

- F16P1_PIG

UniProt

P00636 - F16P1_PIG

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Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain (By similarity).By similarity

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+4 PublicationsNote: Binds 3 Mg(2+) ions per subunit.4 Publications

Enzyme regulationi

Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.6 Publications

Kineticsi

  1. KM=1.2 µM for fructose-1,6-diphosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Magnesium 11 Publication
Metal bindingi98 – 981Magnesium 11 Publication
Metal bindingi98 – 981Magnesium 21 Publication
Metal bindingi119 – 1191Magnesium 21 Publication
Metal bindingi119 – 1191Magnesium 31 Publication
Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygen1 Publication
Metal bindingi122 – 1221Magnesium 31 Publication
Binding sitei141 – 1411AMP1 Publication
Binding sitei265 – 2651Substrate
Metal bindingi281 – 2811Magnesium 31 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225AMP1 Publication
Nucleotide bindingi28 – 325AMP1 Publication
Nucleotide bindingi113 – 1142AMP1 Publication

GO - Molecular functioni

  1. AMP binding Source: UniProtKB
  2. fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB
  4. monosaccharide binding Source: UniProtKB

GO - Biological processi

  1. cellular response to drug Source: UniProtKB
  2. cellular response to magnesium ion Source: UniProtKB
  3. dephosphorylation Source: UniProtKB
  4. fructose 6-phosphate metabolic process Source: UniProtKB
  5. gluconeogenesis Source: UniProtKB
  6. negative regulation of cell growth Source: UniProtKB
  7. negative regulation of glycolytic process Source: UniProtKB
  8. negative regulation of Ras protein signal transduction Source: UniProtKB
  9. protein homotetramerization Source: UniProtKB
  10. regulation of gluconeogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.11. 6170.
SABIO-RKP00636.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
Short name:
FBPase 1
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Liver FBPase
Gene namesi
Name:FBP1
Synonyms:FBP
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551A → L: Destabilizes the inactive T-state and promotes transition to the R-state.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine2 Publications
Modified residuei151 – 1511N6-succinyllysineBy similarity
Modified residuei208 – 2081Phosphoserine; by PKA1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00636.
PRIDEiP00636.

Interactioni

Subunit structurei

Homotetramer.9 Publications

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Helixi30 – 5021Combined sources
Turni51 – 566Combined sources
Beta strandi59 – 646Combined sources
Beta strandi66 – 683Combined sources
Beta strandi70 – 723Combined sources
Helixi73 – 8816Combined sources
Beta strandi92 – 976Combined sources
Beta strandi101 – 1055Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 12212Combined sources
Helixi124 – 1263Combined sources
Turni127 – 1304Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi147 – 1493Combined sources
Helixi150 – 1534Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 17818Combined sources
Beta strandi181 – 1888Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi208 – 2114Combined sources
Helixi214 – 2196Combined sources
Helixi222 – 23211Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi242 – 2454Combined sources
Helixi249 – 25911Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi268 – 2703Combined sources
Turni271 – 2733Combined sources
Beta strandi275 – 2773Combined sources
Turni278 – 2814Combined sources
Helixi282 – 29110Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi299 – 3024Combined sources
Helixi303 – 3053Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi317 – 3204Combined sources
Helixi322 – 33413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CNQX-ray2.27A2-338[»]
1EYIX-ray2.32A2-338[»]
1EYJX-ray2.28A/B2-338[»]
1EYKX-ray2.23A/B2-338[»]
1FBCX-ray2.60A/B2-336[»]
1FBDX-ray2.90A/B2-336[»]
1FBEX-ray3.00A/B2-336[»]
1FBFX-ray2.70A/B2-336[»]
1FBGX-ray3.00A/B2-336[»]
1FBHX-ray2.50A/B2-336[»]
1FBPX-ray2.50A/B2-336[»]
1FJ6X-ray2.50A2-338[»]
1FJ9X-ray2.50A/B2-338[»]
1FPBX-ray2.60A/B2-336[»]
1FPDX-ray2.10A/B2-336[»]
1FPEX-ray2.20A/B2-336[»]
1FPFX-ray2.10A/B2-336[»]
1FPGX-ray2.30A/B2-336[»]
1FPIX-ray2.30A/B2-336[»]
1FPJX-ray2.20A/B2-336[»]
1FPKX-ray3.00A/B2-336[»]
1FPLX-ray2.30A/B2-336[»]
1FRPX-ray2.00A/B2-336[»]
1FSAX-ray2.30A/B2-338[»]
1KZ8X-ray2.00A/F2-338[»]
1LEVX-ray2.15A/F2-338[»]
1NUWX-ray1.30A2-338[»]
1NUXX-ray1.60A2-338[»]
1NUYX-ray1.30A2-338[»]
1NUZX-ray1.90A2-338[»]
1NV0X-ray1.80A2-338[»]
1NV1X-ray1.90A2-338[»]
1NV2X-ray2.10A2-338[»]
1NV3X-ray2.00A2-338[»]
1NV4X-ray1.90A2-338[»]
1NV5X-ray1.90A2-338[»]
1NV6X-ray2.15A2-338[»]
1NV7X-ray2.15A/B2-338[»]
1Q9DX-ray2.35A/B2-338[»]
1RDXX-ray2.75A/B2-338[»]
1RDYX-ray2.20A/B2-338[»]
1RDZX-ray2.05A/B2-338[»]
1YXIX-ray2.00A2-338[»]
1YYZX-ray1.85A2-338[»]
1YZ0X-ray2.07A/B2-338[»]
2F3BX-ray1.80A1-338[»]
2F3DX-ray1.83A1-338[»]
2FBPX-ray2.80A/B2-336[»]
2QVUX-ray1.50A/B2-338[»]
2QVVX-ray2.03A/B2-338[»]
3FBPX-ray2.80A/B2-336[»]
4FBPX-ray2.50A/B/C/D2-336[»]
4GBVX-ray2.90A2-336[»]
4GBWX-ray2.00A2-336[»]
4GWSX-ray2.75A/B2-338[»]
4GWUX-ray3.00A2-338[»]
4GWWX-ray3.20A2-338[»]
4GWXX-ray2.35A2-338[»]
4GWYX-ray3.00A2-338[»]
4GWZX-ray2.60A/B2-338[»]
4GX3X-ray2.25A/B2-338[»]
4GX4X-ray2.50A/B2-338[»]
4GX6X-ray2.50A/B2-338[»]
4H45X-ray3.10A2-338[»]
4H46X-ray2.50A2-338[»]
4KXPX-ray2.70A/B1-338[»]
5FBPX-ray2.10A/B2-336[»]
ProteinModelPortaliP00636.
SMRiP00636. Positions 7-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00636.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1254Substrate binding
Regioni213 – 2164Substrate binding
Regioni244 – 2496Substrate binding
Regioni275 – 2773Substrate binding

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

eggNOGiCOG0158.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP00636.
KOiK03841.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00636-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR
60 70 80 90 100
KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED
110 120 130 140 150
KNAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE
160 170 180 190 200
KDALQPGRNL VAAGYALYGS ATMLVLAMVN GVNCFMLDPA IGEFILVDRD
210 220 230 240 250
VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK
310 320 330
EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK
Length:338
Mass (Da):36,779
Last modified:January 23, 2007 - v4
Checksum:i610BF8D3C6D320F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → A AA sequence (PubMed:6291465)Curated
Sequence conflicti4 – 41Q → E AA sequence (PubMed:6291465)Curated
Sequence conflicti21 – 211E → Q AA sequence (PubMed:6296821)Curated
Sequence conflicti97 – 971S → T AA sequence (PubMed:6296821)Curated
Sequence conflicti157 – 1571G → E AA sequence (PubMed:6296821)Curated
Sequence conflicti200 – 2001D → N AA sequence (PubMed:6296821)Curated
Sequence conflicti229 – 2291Q → E AA sequence (PubMed:6296821)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86347 mRNA. Translation: AAA31035.1.
PIRiS37696. PAPGF.
RefSeqiNP_999144.1. NM_213979.1.
UniGeneiSsc.5127.

Genome annotation databases

GeneIDi397038.
KEGGissc:397038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86347 mRNA. Translation: AAA31035.1 .
PIRi S37696. PAPGF.
RefSeqi NP_999144.1. NM_213979.1.
UniGenei Ssc.5127.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CNQ X-ray 2.27 A 2-338 [» ]
1EYI X-ray 2.32 A 2-338 [» ]
1EYJ X-ray 2.28 A/B 2-338 [» ]
1EYK X-ray 2.23 A/B 2-338 [» ]
1FBC X-ray 2.60 A/B 2-336 [» ]
1FBD X-ray 2.90 A/B 2-336 [» ]
1FBE X-ray 3.00 A/B 2-336 [» ]
1FBF X-ray 2.70 A/B 2-336 [» ]
1FBG X-ray 3.00 A/B 2-336 [» ]
1FBH X-ray 2.50 A/B 2-336 [» ]
1FBP X-ray 2.50 A/B 2-336 [» ]
1FJ6 X-ray 2.50 A 2-338 [» ]
1FJ9 X-ray 2.50 A/B 2-338 [» ]
1FPB X-ray 2.60 A/B 2-336 [» ]
1FPD X-ray 2.10 A/B 2-336 [» ]
1FPE X-ray 2.20 A/B 2-336 [» ]
1FPF X-ray 2.10 A/B 2-336 [» ]
1FPG X-ray 2.30 A/B 2-336 [» ]
1FPI X-ray 2.30 A/B 2-336 [» ]
1FPJ X-ray 2.20 A/B 2-336 [» ]
1FPK X-ray 3.00 A/B 2-336 [» ]
1FPL X-ray 2.30 A/B 2-336 [» ]
1FRP X-ray 2.00 A/B 2-336 [» ]
1FSA X-ray 2.30 A/B 2-338 [» ]
1KZ8 X-ray 2.00 A/F 2-338 [» ]
1LEV X-ray 2.15 A/F 2-338 [» ]
1NUW X-ray 1.30 A 2-338 [» ]
1NUX X-ray 1.60 A 2-338 [» ]
1NUY X-ray 1.30 A 2-338 [» ]
1NUZ X-ray 1.90 A 2-338 [» ]
1NV0 X-ray 1.80 A 2-338 [» ]
1NV1 X-ray 1.90 A 2-338 [» ]
1NV2 X-ray 2.10 A 2-338 [» ]
1NV3 X-ray 2.00 A 2-338 [» ]
1NV4 X-ray 1.90 A 2-338 [» ]
1NV5 X-ray 1.90 A 2-338 [» ]
1NV6 X-ray 2.15 A 2-338 [» ]
1NV7 X-ray 2.15 A/B 2-338 [» ]
1Q9D X-ray 2.35 A/B 2-338 [» ]
1RDX X-ray 2.75 A/B 2-338 [» ]
1RDY X-ray 2.20 A/B 2-338 [» ]
1RDZ X-ray 2.05 A/B 2-338 [» ]
1YXI X-ray 2.00 A 2-338 [» ]
1YYZ X-ray 1.85 A 2-338 [» ]
1YZ0 X-ray 2.07 A/B 2-338 [» ]
2F3B X-ray 1.80 A 1-338 [» ]
2F3D X-ray 1.83 A 1-338 [» ]
2FBP X-ray 2.80 A/B 2-336 [» ]
2QVU X-ray 1.50 A/B 2-338 [» ]
2QVV X-ray 2.03 A/B 2-338 [» ]
3FBP X-ray 2.80 A/B 2-336 [» ]
4FBP X-ray 2.50 A/B/C/D 2-336 [» ]
4GBV X-ray 2.90 A 2-336 [» ]
4GBW X-ray 2.00 A 2-336 [» ]
4GWS X-ray 2.75 A/B 2-338 [» ]
4GWU X-ray 3.00 A 2-338 [» ]
4GWW X-ray 3.20 A 2-338 [» ]
4GWX X-ray 2.35 A 2-338 [» ]
4GWY X-ray 3.00 A 2-338 [» ]
4GWZ X-ray 2.60 A/B 2-338 [» ]
4GX3 X-ray 2.25 A/B 2-338 [» ]
4GX4 X-ray 2.50 A/B 2-338 [» ]
4GX6 X-ray 2.50 A/B 2-338 [» ]
4H45 X-ray 3.10 A 2-338 [» ]
4H46 X-ray 2.50 A 2-338 [» ]
4KXP X-ray 2.70 A/B 1-338 [» ]
5FBP X-ray 2.10 A/B 2-336 [» ]
ProteinModelPortali P00636.
SMRi P00636. Positions 7-338.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P00636.
ChEMBLi CHEMBL2263.

Proteomic databases

PaxDbi P00636.
PRIDEi P00636.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397038.
KEGGi ssc:397038.

Organism-specific databases

CTDi 2203.

Phylogenomic databases

eggNOGi COG0158.
HOGENOMi HOG000191265.
HOVERGENi HBG005627.
InParanoidi P00636.
KOi K03841.

Enzyme and pathway databases

UniPathwayi UPA00138 .
BRENDAi 3.1.3.11. 6170.
SABIO-RK P00636.

Miscellaneous databases

EvolutionaryTracei P00636.

Family and domain databases

HAMAPi MF_01855. FBPase_class1.
InterProi IPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view ]
PANTHERi PTHR11556. PTHR11556. 1 hit.
Pfami PF00316. FBPase. 1 hit.
[Graphical view ]
PIRSFi PIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSi PR00115. F16BPHPHTASE.
PROSITEi PS00124. FBPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase."
    Williams M.K., Kantrowitz E.R.
    Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase."
    Marcus F., Edelstein I., Reardon I., Heinrikson R.L.
    Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-336, ACETYLATION AT THR-2, PHOSPHORYLATION AT SER-208.
    Tissue: Kidney cortex.
  3. "Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases."
    McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L.
    Arch. Biochem. Biophys. 217:652-664(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24 AND 44-61, ACETYLATION AT THR-2.
    Tissue: Kidney.
  4. "Mechanism of action of fructose 1,6-bisphosphatase."
    Benkovic S.J., Demaine M.M.
    Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING SITE, LIGANDS, REVIEW.
  5. "Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8-A resolution."
    Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.
    J. Mol. Biol. 212:513-539(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE, SEQUENCE REVISION.
  6. "Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium."
    Ke H.M., Zhang Y.P., Lipscomb W.N.
    Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE; AMP AND MAGNESIUM, ENZYME REGULATION, SUBUNIT.
  7. "Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution."
    Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N.
    Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
  8. "Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution."
    Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N.
    Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE.
  9. "Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase."
    Choe J.-Y., Poland B.W., Fromm H.J., Honzatko R.B.
    Biochemistry 37:11441-11450(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR, ENZYME REGULATION.
  10. "Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes."
    Choe J.-Y., Fromm H.J., Honzatko R.B.
    Biochemistry 39:8565-8574(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; PHOSPHATE; AMP; MAGNESIUM AND ZINC IONS, SUBUNIT, ENZYME REGULATION.
  11. "Metaphosphate in the active site of fructose-1,6-bisphosphatase."
    Choe J.-Y., Iancu C.V., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 278:16015-16020(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS; FRUCTOSE-6-PHOSPHATE AND PHOSPHATE, COFACTOR, ENZYME MECHANISM.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH THE SYNTHETIC INHIBITOR OC252; FRUCTOSE-6-PHOSPHATE; PHOSPHATE AND DIVALENT METAL CATIONS, COFACTOR, SUBUNIT, ENZYME REGULATION.
  13. "R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase."
    Iancu C.V., Mukund S., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 280:19737-19745(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT LEU-55 IN COMPLEXES WITH AMP; FRUCTORSE-6-PHOSPHAT; PHOSPHATE AND MAGNESIUM IONS, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  14. "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition."
    Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.
    J. Biol. Chem. 282:36121-36131(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS AND FRUCTOSE-2,6-DIPHOSPHATE, SUBUNIT, ENZYME REGULATION.

Entry informationi

Entry nameiF16P1_PIG
AccessioniPrimary (citable) accession number: P00636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g. with homocystine) but is not essential for enzyme activity.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3